Results 41 to 50 of about 20,996 (256)
The triphenylmethane dye brilliant blue G is only moderately effective at inhibiting amyloid formation by human amylin or at disaggregating amylin amyloid fibrils, but interferes with amyloid assays; Implications for inhibitor design. [PDF]
, 2019 The development of inhibitors of islet amyloid formation is important as pancreatic amyloid deposition contributes to type-2 diabetes and islet transplant failure.
Akter, Rehana +4 more
core +3 more sources
Angewandte Chemie, 2020 Amyloid self‐assembly of islet amyloid polypeptide (IAPP) is linked to pancreatic inflammation, β‐cell degeneration, and the pathogenesis of type 2 diabetes (T2D).
Valentina Armiento +5 more
semanticscholar +1 more source
Matrix Metalloproteinase-9 Reduces Islet Amyloid Formation by Degrading Islet Amyloid Polypeptide [PDF]
Journal of Biological Chemistry, 2013 Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation.
Kathryn, Aston-Mourney +6 more
openaire +2 more sources
Scientific Reports, 2017 Type 2 diabetes is characterized by insulin tolerance in target cells followed by a reduction of pancreatic β-cell mass. Islet amyloid polypeptide oligomeric assemblies were shown to contribute to β-cell apoptosis by forming discrete pores that ...
Yaron Bram +4 more
doaj +1 more source
Anatomic and molecular characterization of the 1 endocrine pancreas of a teleostean fish: Atlantic wolffish (Anarhichas lupus) [PDF]
, 2015 Background: The biologic attributes of the endocrine pancreas and the comparative endocrinology of islet amyloid polypeptide (IAPP) of fish are not well described in the literature.
Benoit-Biancamano, Marie-Odile +4 more
core +1 more source
Frontiers in Chemistry, 2020 Protein aggregation, involving the formation of dimers, oligomers, and fibrils, is associated with many human diseases. Type 2 diabetes is one of the common amyloidosis and linked with the aggregation of human islet amyloid polypeptide (hIAPP).
Cuiqin Bai +4 more
semanticscholar +1 more source
Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis
Journal of Diabetes Research, 2015 Type II diabetes mellitus is associated with the deposition of fibrillar aggregates in pancreatic islets. The major protein component of islet amyloids is the glucomodulatory hormone islet amyloid polypeptide (IAPP).
Phuong Trang Nguyen +3 more
doaj +1 more source
Fibril Structure of Human Islet Amyloid Polypeptide [PDF]
Journal of Biological Chemistry, 2012 Misfolding and amyloid fibril formation by human islet amyloid polypeptide (hIAPP) are thought to be important in the pathogenesis of type 2 diabetes, but the structures of the misfolded forms remain poorly understood. Here we developed an approach that combines site-directed spin labeling with continuous wave and pulsed EPR to investigate local ...
Sahar, Bedrood +6 more
openaire +2 more sources
Degradation of islet amyloid polypeptide by neprilysin [PDF]
Diabetologia, 2012 A progressive loss of pancreatic beta cell function, a decrease in beta cell mass and accumulation of islet amyloid is characteristic of type 2 diabetes mellitus. The main constituent of islet amyloid is islet amyloid polypeptide (IAPP). In this study, we examined the ability of the peptidase neprilysin to cleave IAPP and prevent human IAPP-induced ...
H, Guan +4 more
openaire +2 more sources
Foldamer-mediated manipulation of a pre-amyloid toxin
Nature Communications, 2016 Intrinsically disordered proteins that form amyloid fibrils are hard to target with traditional therapeutic approaches. Here, the authors report on an oligoquinoline derivative that binds the human islet amyloid polypeptide, stabilising an alpha-helical ...
Sunil Kumar +5 more
doaj +1 more source